ID   ADAT1_MACFA             Reviewed;         502 AA.
AC   Q4R7N3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=tRNA-specific adenosine deaminase 1;
DE            EC=3.5.4.34;
DE   AltName: Full=tRNA-specific adenosine-37 deaminase;
GN   Name=ADAT1; ORFNames=QtsA-14745;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in
CC         tRNA(Ala) + NH4(+); Xref=Rhea:RHEA:50968, Rhea:RHEA-COMP:12855,
CC         Rhea:RHEA-COMP:12856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.34;
CC   -!- COFACTOR:
CC       Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
CC       {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the ADAT1 family. {ECO:0000305}.
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DR   EMBL; AB168782; BAE00889.1; -; mRNA.
DR   RefSeq; NP_001270373.1; NM_001283444.1.
DR   AlphaFoldDB; Q4R7N3; -.
DR   SMR; Q4R7N3; -.
DR   STRING; 9541.XP_005592642.1; -.
DR   GeneID; 101925428; -.
DR   CTD; 23536; -.
DR   eggNOG; KOG2777; Eukaryota.
DR   OrthoDB; 947117at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; ISS:UniProtKB.
DR   GO; GO:0008033; P:tRNA processing; ISS:UniProtKB.
DR   InterPro; IPR002466; A_deamin.
DR   Pfam; PF02137; A_deamin; 1.
DR   SMART; SM00552; ADEAMc; 1.
DR   PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Phosphoprotein; Reference proteome;
KW   tRNA processing; Zinc.
FT   CHAIN           1..502
FT                   /note="tRNA-specific adenosine deaminase 1"
FT                   /id="PRO_0000287647"
FT   DOMAIN          63..501
FT                   /note="A to I editase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   ACT_SITE        89
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         93
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         302
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         470
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHI2"
SQ   SEQUENCE   502 AA;  55490 MW;  7B4C08EEB9B8E4BF CRC64;
     MWTADEIALL CYEHYGIRLP KKGKPEPNHE WTLLAAVVKI QSPADQDCDT PDKPAQVTKE
     VVSMGTGTKC IGQSKMRKSG DILNDSHAEV IARRNFQRYL LHQLQLAATL KEDSIFVPGT
     QKGLWKLRRD LFFVFFSSHT PCGDASIIPM LEFEDQPCCP VIRDWASSSS VEASSNLEAP
     GNERKCEDLD SPVTKKMRLE PMTAAREVTN GATHHQSFGK QESGPISPGI NSCNLTVEGL
     AAVTRIAPGS AKVIDVYRTG AKCVPGEAGD SRKPGAAFHQ VGLLRVKPGR GDRTRSMSCS
     DKMARWNVLG CQGALLMHFL EEPIYLSAVV IGKCPYSQEA MQRALTGRRQ NVSALPKGFG
     VQELKILQSD LLFEQSRCAV QAKRADSPGR LVPCGAAISW SAVPEQPLDV TANGFPQGTT
     KKTIGSLQAR SQISKVELLR SFQKLLSRIA RDKWPDSLRV QKLDTYQDYK EAASSYQEAW
     STLRKQAFGS WIRNPPDYHQ FK